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Database: UniProt
Entry: A5EW54
LinkDB: A5EW54
Original site: A5EW54 
ID   ALR_DICNV               Reviewed;         357 AA.
AC   A5EW54;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   16-JAN-2019, entry version 72.
DE   RecName: Full=Alanine racemase {ECO:0000255|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN   Name=alr; OrderedLocusNames=DNO_0325;
OS   Dichelobacter nodosus (strain VCS1703A).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cardiobacteriales;
OC   Cardiobacteriaceae; Dichelobacter.
OX   NCBI_TaxID=246195;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VCS1703A;
RX   PubMed=17468768; DOI=10.1038/nbt1302;
RA   Myers G.S.A., Parker D., Al-Hasani K., Kennan R.M., Seemann T.,
RA   Ren Q., Badger J.H., Selengut J.D., Deboy R.T., Tettelin H.,
RA   Boyce J.D., McCarl V.P., Han X., Nelson W.C., Madupu R., Mohamoud Y.,
RA   Holley T., Fedorova N., Khouri H., Bottomley S.P., Whittington R.J.,
RA   Adler B., Songer J.G., Rood J.I., Paulsen I.T.;
RT   "Genome sequence and identification of candidate vaccine antigens from
RT   the animal pathogen Dichelobacter nodosus.";
RL   Nat. Biotechnol. 25:569-575(2007).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. May also act on other amino acids. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249,
CC         ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01201};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01201};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01201}.
DR   EMBL; CP000513; ABQ13078.1; -; Genomic_DNA.
DR   RefSeq; WP_012030669.1; NC_009446.1.
DR   ProteinModelPortal; A5EW54; -.
DR   SMR; A5EW54; -.
DR   STRING; 246195.DNO_0325; -.
DR   EnsemblBacteria; ABQ13078; ABQ13078; DNO_0325.
DR   KEGG; dno:DNO_0325; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031446; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   OrthoDB; 859043at2; -.
DR   BioCyc; DNOD246195:G1G7U-322-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000248; Chromosome.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 1.
DR   HAMAP; MF_01201; Ala_racemase; 1.
DR   InterPro; IPR000821; Ala_racemase.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR011079; Ala_racemase_C.
DR   InterPro; IPR001608; Ala_racemase_N.
DR   InterPro; IPR020622; Ala_racemase_pyridoxalP-BS.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   Pfam; PF00842; Ala_racemase_C; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   PRINTS; PR00992; ALARACEMASE.
DR   SMART; SM01005; Ala_racemase_C; 1.
DR   SUPFAM; SSF50621; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR00492; alr; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Isomerase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    357       Alanine racemase.
FT                                /FTId=PRO_1000065987.
FT   ACT_SITE     34     34       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    252    252       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     127    127       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     301    301       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      34     34       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   357 AA;  39491 MW;  B9235EA0F77C246F CRC64;
     MRALKKIINL NALRHNWALI KQRSLPATPM VVLKADAYGH GMTTVAKTLD DARYFAVSCI
     EEAIALRHLG IDTPVVLLEG VYRADELLLC EYYQFDTLVH NFRQMQWLKE FNGSVKAWLK
     VDSGMHRLGF TQDEIAEAFA QAHSLPVNIQ WQGVITHFAC SDEDDLTHAK KQLACMDRLV
     LPAHWKRCYA NSAAIFALPQ AHYDYTRSGI MLYGLSPFMH GDGSAYGLQP VMTVITEILA
     VRHLEKNETA GYGQGFTAPE SGWLATIALG YGDGFARTIT SGAVPVLIAG QRYPLVGRVA
     MDMAMVWLGS DRYAEGTIVE LFGSHLPTEE VARAAGTIPH TLTTMLMPRV HVEIVGG
//
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